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Originally published In Press as doi:10.1074/jbc.M005506200 on July 27, 2000

J. Biol. Chem., Vol. 275, Issue 40, 31099-31106, October 6, 2000
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Activation of Protein Kinase C Stimulates the Dephosphorylation of Natriuretic Peptide Receptor-B at a Single Serine Residue
A POSSIBLE MECHANISM OF HETEROLOGOUS DESENSITIZATION*

Lincoln R. PotterDagger and Tony Hunter§

From the Molecular Biology and Virology Laboratory, The Salk Institute for Biological Studies, La Jolla, California 92037

The binding of atrial natriuretic peptide and C-type natriuretic peptide (CNP) to the guanylyl cyclase-linked natriuretic peptide receptors A and B (NPR-A and -B), respectively, stimulates increases in intracellular cGMP concentrations. The vasoactive peptides vasopressin, angiotensin II, and endothelin inhibit natriuretic peptide-dependent cGMP elevations by activating protein kinase C (PKC). Recently, we identified six in vivo phosphorylation sites for NPR-A and five sites for NPR-B and demonstrated that the phosphorylation of these sites is required for ligand-dependent receptor activation. Here, we show that phorbol 12-myristate 13-acetate, a direct activator of PKC, causes the dephosphorylation and desensitization of NPR-B. In contrast to the CNP-dependent desensitization process, which results in coordinate dephosphorylation of all five sites in the receptor, phorbol 12-myristate 13-acetate treatment causes the dephosphorylation of only one site, which we have identified as Ser523. The conversion of this residue to alanine or glutamate did not reduce the amount of mature receptor protein as indicated by detergent-dependent guanylyl cyclase activities or Western blot analysis but completely blocked the ability of PKC to induce the dephosphorylation and desensitization of NPR-B. Thus, in contrast to previous reports suggesting that PKC directly phosphorylates and inhibits guanylyl cyclase-linked natriuretic peptide receptors, we show that PKC-dependent dephosphorylation of NPR-B at Ser523 provides a possible molecular explanation for how pressor hormones inhibit CNP signaling.

* This work was supported by United States Public Health Service Grants CA14195 and CA39780 (to T. H.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Supported by National Research Service Award CA-67452 from the National Cancer Institute. To whom correspondence should be addressed. Dept. of Biochemistry, Molecular Biology and Biophysics, University of Minnesota-Twin Cities, 356 Gortner Laboratory, 1479 Gortner Ave., St. Paul, MN 55108. Tel.: 612-624-7251; Fax: 612-624-7282; E-mail: Potter@tc.umn.edu.

§ Frank and Else Schilling American Cancer Society Research Professor.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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